Isolation of two endo-beta-N-acetylglucosaminidases from fig latex.
Two endo-beta-N-acetylglucosaminidases (mannosyl-glycoprotein 1,4-N-acetamidodeoxy-beta-D-glycohydrolase, EC 3.2.1.96) (type F-I and type F-II) have been isolated from fig latex. At pH 7.0, type F-1 was retained by the DEAE-Sephadex A-50 column, whereas type F-II was not adsorbed by the column. The optimum pH of type F-I was found to be pH 5.9 and type F-II, pH 5.4. Type F-I enzyme hydrolyzes the tri-mannosyl derivatives di-N-acetylglucosaminylasparagine faster than the penta- or hexa-mannosyl compounds. Type F-II hydrolyzes the penta- and hexa-mannosyl derivatives, but not the tri-mannosyl compound.
D000118:Acetylglucosaminidase / Q000302:isolation & purification / Q000378:metabolism*; D004355:Drug Stability; D006020:Glycopeptides / Q000378:metabolism; D006596:Hexosaminidases / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007840:Latex / Q000032:analysis*; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008970:Molecular Weight; D010944:Plants / Q000201:enzymology*; D013379:Substrate Specificity
D006020:Glycopeptides; D007840:Latex; D006596:Hexosaminidases; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase